4-methoxy-3-methyl-2-phytyl-1-naphthalenol | 81818-55-5

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 异戊烯醇脂质
• 英文名称: 4-methoxy-3-methyl-2-phytyl-1-naphthalenol
• 英文别名: 4-methoxy-3-methyl-2-(3,7,11,15-tetramethylhexadec-2-enyl)naphthalen-1-ol
• CAS: 81818-55-5
• 化学式: C₃₂H₅₀O₂
• 分子量: 466.748
• InChiKey: KYPLNSROCQFWIH-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  9.79
• 重原子数：
  34.0
• 可旋转键数：
  15.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.62
• 拓扑面积：
  29.46
• 氢给体数：
  1.0
• 氢受体数：
  2.0

反应信息

• 作为反应物：
  描述：

  4-methoxy-3-methyl-2-phytyl-1-naphthalenol 在 ammonium cerium(IV) nitrate 、 重氧水 作用下， 以 乙腈 为溶剂， 反应 0.33h， 生成 维生素k 、 vitamin K 、 vitamin K-1-18O
  参考文献：
  名称：

  The Active Site of Vitamin K and the Role of the Vitamin K-Dependent Carboxylase

  摘要：

  Vitamin K is the blood-clotting vitamin. It participates in the blood coagulation cascade as a carboxylase cofactor. Enzymic oxygenation of vitamin K hydroquinone provides the driving force for the carboxylation of selected glutamates in the proteins of the blood-clotting cascade. The active site of vitamin K has now been defined by O-18-labeling experiments. The oxygenation is completely specific for the carbonyl group adjacent to the quinone methyl group of vitamin K. The experiment makes use of the O-18-labeled vitamin K isotopomers 9 and 10. Thus, oxygenation of 9 with O-16(2) occurs at the carbonyl group next to methyl, as shown by exchange of the O-18 label at that position. Synthesis of the two O-18-labeled vitamin K isotopomers 9 and 10 was accomplished by cerium(IV)-mediated oxidation in the presence of (H2O)-O-18 of the corresponding methyl half-ethers 4 and 8. The position of the label was ascertained by C-13 and heteronuclear NOE NMR spectroscopies. A role for the active site thiols on the vitamin K-dependent carboxylase is also suggested. The thiolate anion is an excellent candidate for the weak base that initiates the base strength amplification sequence leading to carboxylation and vitamin K oxide formation.

  DOI：

  10.1021/ja00101a003
• 作为产物：
  描述：

  4-acetoxy-1-methoxy-2-methyl-3-phytylnaphthalene 在 sodium hydroxide 作用下， 以 乙醇 为溶剂， 反应 0.75h， 生成 4-methoxy-3-methyl-2-phytyl-1-naphthalenol
  参考文献：
  名称：

  The Active Site of Vitamin K and the Role of the Vitamin K-Dependent Carboxylase

  摘要：

  Vitamin K is the blood-clotting vitamin. It participates in the blood coagulation cascade as a carboxylase cofactor. Enzymic oxygenation of vitamin K hydroquinone provides the driving force for the carboxylation of selected glutamates in the proteins of the blood-clotting cascade. The active site of vitamin K has now been defined by O-18-labeling experiments. The oxygenation is completely specific for the carbonyl group adjacent to the quinone methyl group of vitamin K. The experiment makes use of the O-18-labeled vitamin K isotopomers 9 and 10. Thus, oxygenation of 9 with O-16(2) occurs at the carbonyl group next to methyl, as shown by exchange of the O-18 label at that position. Synthesis of the two O-18-labeled vitamin K isotopomers 9 and 10 was accomplished by cerium(IV)-mediated oxidation in the presence of (H2O)-O-18 of the corresponding methyl half-ethers 4 and 8. The position of the label was ascertained by C-13 and heteronuclear NOE NMR spectroscopies. A role for the active site thiols on the vitamin K-dependent carboxylase is also suggested. The thiolate anion is an excellent candidate for the weak base that initiates the base strength amplification sequence leading to carboxylation and vitamin K oxide formation.

  DOI：

  10.1021/ja00101a003

文献信息

• The Active Site of Vitamin K and the Role of the Vitamin K-Dependent Carboxylase
  作者：Sriram Naganathan、Roger Hershline、Seung Wook Ham、Paul Dowd

  DOI：10.1021/ja00101a003

  日期：1994.11

  Vitamin K is the blood-clotting vitamin. It participates in the blood coagulation cascade as a carboxylase cofactor. Enzymic oxygenation of vitamin K hydroquinone provides the driving force for the carboxylation of selected glutamates in the proteins of the blood-clotting cascade. The active site of vitamin K has now been defined by O-18-labeling experiments. The oxygenation is completely specific for the carbonyl group adjacent to the quinone methyl group of vitamin K. The experiment makes use of the O-18-labeled vitamin K isotopomers 9 and 10. Thus, oxygenation of 9 with O-16(2) occurs at the carbonyl group next to methyl, as shown by exchange of the O-18 label at that position. Synthesis of the two O-18-labeled vitamin K isotopomers 9 and 10 was accomplished by cerium(IV)-mediated oxidation in the presence of (H2O)-O-18 of the corresponding methyl half-ethers 4 and 8. The position of the label was ascertained by C-13 and heteronuclear NOE NMR spectroscopies. A role for the active site thiols on the vitamin K-dependent carboxylase is also suggested. The thiolate anion is an excellent candidate for the weak base that initiates the base strength amplification sequence leading to carboxylation and vitamin K oxide formation.